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Lamin A/C Proteins (LMNA)

On www.antibodies-online.com are 16 Lamin A/C (LMNA) Proteins from 9 different suppliers available. Additionally we are shipping Lamin A/C Antibodies (473) and Lamin A/C Kits (30) and many more products for this protein. A total of 537 Lamin A/C products are currently listed.

More Proteins for Lamin A/C Interaction Partners

Human Lamin A/C (LMNA) interaction partners

some LMNA mutations may be associated with a favourable prognosis and a low risk of sudden death. Protein expression studies suggested that a severe outcome was associated with the expression of high amounts of mutated protein.

ZMPSTE24-dependent cleavage of prelamin A and the eight known disease-associated ZMPSTE24 missense mutations, were examined.

The LMNA-NTRK1 fusion was likely the molecular driver of tumorigenesis and metastasis in this patient, and the observed effectiveness of crizotinib treatment provides clinical validation of this molecular target.

The functional integrity of lamin and nesprin-1 is thus required to modulate the FHOD1 activity and the inside-out mechanical coupling that tunes the cell internal stiffness to match that of its soft, physiological-like environment.

The role of 1B and 2B domains in modulating elastic properties of lamin A.

progerin is upregulated in human dilated cardiomyopathy hearts and strongly correlates with left ventricular remodeling

Data indicate that patients with truncation mutations in LMNA (lamin A/C) had an earlier occurrence of cardiac conduction disturbance and low left ventricular ejection fraction, than those with missense mutations.

A novel truncating LMNA mutation associated with Cardiac conduction disorders and dilated cardiomyopathy was discovered in this family characterized by gender differences in clinical severity in LMNA carriers

We find no evidence for an elevated mutation rate in progerin-expressing cells. We conclude that the cellular defect in HGPS cells does not lie in the repair of DNA damage per se.

pathogenic gene mutations in LMNA and MYBPC3 alter RNA splicing and may have a role in heart disease

Patients with the heterozygous LMNA p.T10I mutation have distinct clinical features and significantly worse metabolic complications compared with other patients with atypical progeroid syndrome as well as patients with Hutchinson-Gilford progeria syndrome.

Mouse (Murine) Lamin A/C (LMNA) interaction partners

we show that the H222P amino acid substitution in lamin A enhances its binding to ERK1/2 and increases sequestration at the nuclear envelope. Finally, we show that genetic deletion of Dusp4 has beneficial effects on heart function and prolongs survival in LmnaH222P/H222P mice. These results further establish Dusp4 as a key contributor to the pathogenesis of LMNA cardiomyopathy and a potential target for drug therapy.

Data show that lamin A/C expressing cells can form an actin cap to resist nuclear deformation in response to physiological mechanical stresses.

THE ROLE OF LMNA MUTATIONS IN MYOGENIC DIFFERENTIATION OF PRIMARY SATELLITE CELLS AND C2C12 CELLS.

Itm2a knockdown is sufficient to rescue the inhibitory effects of lamin A WT and R482W mutant overexpression on 3T3-L1 differentiation.

our findings indicate that altered mTOR signaling in Lmna(-/-) mice leads to a lipodystrophic phenotype that can be rescued with rapamycin, highlighting the effect of loss of adipose tissue in Lmna(-/-) mice and the consequences of altered mTOR signaling

results suggest that lamin A plays important roles in maintaining the osteoblast differentiation and function

these findings show that cardiac ERK1/2 activity is modulated in part by TGF-b/Smad signaling, leading to altered activation of CTGF/CCN2 to mediate fibrosis and alter cardiac function. This identifies a novel mechanism in the development of LMNA cardiomyopathy.

Activation of WNT/b-catenin activity improved cardiac contractility and ameliorated intraventricular conduction defects in LmnaH222P/H222P mice, which was associated with increased expression of myocardial connexin 43. These results indicate that decreased WNT/b-catenin contributes to the pathophysiology of LMNA cardiomyopathy and that drugs activating b-catenin may be beneficial in affected individuals

SUMO1 conjugation of RB and Lamin A/C is modulated by the SUMO protease SENP1 and that sumoylation of both proteins is required for their interaction.

Lmna-deficient cells show a compromised strain avoidance response, which is completely abolished when topographical cues and uniaxial strain are applied along the same direction.

While the distribution patterns of both lamins closely paralleled the respective stages of mitosis, Nup160 localization in metaphase oocytes corresponded to that in mitotic prometaphase rather than metaphase.

changes in nuclear size and shape, which are mediated by nuclear envelope structural proteins lamin A/C and/or emerin, also impact gene regulation and lineage differentiation in early embryos.

specific laminopathy-associated mutations exhibit both positive and negative effects on prelamin A accumulation, indicating that these mutations affect prelamin A processing efficiency in different manners.

administration of the exon 11 ASO reduced lamin A expression in wild-type mice and progerin expression in an HGPS mouse model.

stabilization of perinuclear actin strengthens the transient interactions of lamin A with chromatin

It was found that the lamin A protein expressed in mouse ear cartilage cells is shorter than protein expressed in mouse skin. This difference in protein length could be caused by differential cleavage in the cells of skin and ear cartilage tissues

developmental disorders caused by lesions in the B-type lamins and interacting proteins

Zebrafish Lamin A/C (LMNA) interaction partners

results have important implications for understanding the tissue-specific regulation and functions of the lamin A gene

The induction of embryonic senescence and laminopathies in zebrafish harboring disturbed expressions of the lamin A gene, is described.

Xenopus laevis Lamin A/C (LMNA) interaction partners

These results indicate that thyroid hormone-regulated expression of nuclear lamin A and LIII closely correlates with dedifferentiation of the epithelial cells in the X. laevis intestine.

LIII filaments appear identical to the endogenous lamina, whereas lamin B2 assembles into filaments that are organized less precisely; Lamin A induces sheets of thicker filaments on the endogenous lamina and increases the rigidity of the nuclear envelope

Ectopic expression of prelamin A in early Xenopus embryos induces apoptosis.

Pig (Porcine) Lamin A/C (LMNA) interaction partners

Both anti-lamin A/C and anti-lamin B staining were clearly present in all embryonic stages.

A study mapping the location of procine lamin type A to chromosome 4q is presented.

Lamin A/C (LMNA) Protein Profile

Protein Summary

The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. Alternative splicing results in multiple transcript variants. Mutations in this gene lead to several diseases: Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.